SitesBLAST
Comparing N515DRAFT_3749 FitnessBrowser__Dyella79:N515DRAFT_3749 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 3 hits to proteins with known functional sites (download)
Q9XBQ8 L-lysine 2,3-aminomutase; LAM; KAM; EC 5.4.3.2 from Clostridium subterminale (see paper)
32% identity, 96% coverage: 16:336/336 of query aligns to 19:340/416 of Q9XBQ8
- E86 (= E82) mutation to Q: Reduction in activity. Decrease in iron and sulfide and PLP content.
- D96 (= D92) mutation to N: Reduction in activity. Decrease in iron and sulfide and PLP content.
- R130 (= R126) mutation R->Q,K: Complete loss of activity. Decrease in iron and sulfide but not PLP content. Destabilise the iron-sulfur centers.
- R134 (= R130) mutation to K: Complete loss of activity. Significant decrease in iron and sulfide and PLP content.; mutation to Q: Complete loss of activity. Slight decrease in iron and sulfide and PLP content.
- R135 (= R131) mutation to K: Reduction in activity. Decrease in iron and sulfide and PLP content.; mutation to Q: Reduction in activity. Significant decrease in iron and sulfide and PLP content.
- R136 (≠ H132) mutation to Q: Reduction in activity. Significant decrease in iron and sulfide and PLP content.
- D165 (≠ E160) mutation to N: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
- D172 (= D167) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content. Destabilise the iron-sulfur centers.
- E236 (= E232) mutation to Q: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
- D293 (= D289) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content.
- D330 (≠ E326) mutation D->A,N: Complete loss of activity. Decrease in iron and sulfide and PLP content.
2a5hB 2.1 angstrom x-ray crystal structure of lysine-2,3-aminomutase from clostridium subterminale sb4, with michaelis analog (l-alpha-lysine external aldimine form of pyridoxal-5'-phosphate). (see paper)
32% identity, 96% coverage: 16:336/336 of query aligns to 17:338/410 of 2a5hB
- active site: R110 (≠ K108), Y111 (= Y109), R114 (= R112), C123 (= C121), C127 (= C125), C130 (= C128), R132 (= R130), D291 (= D289), D328 (≠ E326), K335 (= K333)
- binding lysine: L96 (≠ V94), L116 (= L114), R132 (= R130), L165 (≠ I162), S167 (= S164), Y288 (≠ H286), D291 (= D289), D328 (≠ E326)
- binding pyridoxal-5'-phosphate: T108 (≠ L106), Y111 (= Y109), R114 (= R112), L116 (= L114), R196 (= R193), Y285 (= Y283), Y286 (= Y284), K335 (= K333)
- binding s-adenosylmethionine: H129 (≠ Y127), T131 (≠ F129), R132 (= R130), S167 (= S164), G169 (= G166), G198 (≠ H195), H228 (= H226), Q256 (= Q254), V258 (= V256), Y288 (≠ H286), C290 (≠ L288), D291 (= D289)
- binding iron/sulfur cluster: C123 (= C121), C127 (= C125), C130 (= C128), G169 (= G166), R200 (= R197), H228 (= H226)
Sites not aligning to the query:
O34676 L-lysine 2,3-aminomutase; LAM; KAM; EC 5.4.3.2 from Bacillus subtilis (strain 168) (see paper)
31% identity, 84% coverage: 53:333/336 of query aligns to 66:346/471 of O34676
- K290 (≠ A277) mutation to Q: More than 95% loss of activity, and half of normal PLP binding capacity.
- K346 (= K333) mutation to Q: No activity and no bound PLP.
Sites not aligning to the query:
- 361 K→Q: 95% loss of activity, normal PLP binding capacity.
Query Sequence
>N515DRAFT_3749 FitnessBrowser__Dyella79:N515DRAFT_3749
MITASPAARLLPPAADWRELWRASITDAGELLRTVQLGHLAGRLPPGDAGFALRVPRGFA
ARMRPGDPDDPLLLQVLPQLAELEQAPGYVADPVGDLAAREAQGLLHKYEGRALLIASGS
CAVNCRYCFRRHFPYGEEMAAAGQWRKALDHLRQDASIAELILSGGDPLSLATPKLEELS
RGLAALPQVTRLRIHTRLPVVLPERIDAAFLAWFAALPLQKVVVLHANHANEFDAAVDDA
CRRLREAGATLLNQSVLLKNINDDADTLSELSERLFAAGVLPYYLHQLDRVQGSAHFEVD
DARARALVEAIRGRLPGYLVPKLVREMEGDASKRPV
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory